Figure 1

Human Nek6 and Nek7 structure predictions and sequence aligment. Consensus of predicted secondary structure for Nek6 (A) and Nek7 (B), is represented by helices (red waves), strands (yellow arrows) and coils (black lines); it was generated from 5 different predictions and the consensus score for each amino acid (1-5) is shown (scores 1-2 represent ambiguous predictions). The consensus of predicted disordered regions was generated from 9 predictions; it is represented by blue bars when the consensus score (0-9) is from 5 to 9. The N-terminal regulatory and C-terminal kinase domains are depicted and two key signatures within the kinase domain are in colored boxes as follows: ATP-binding region, green; Ser/Thr kinases active-site, orange. The conserved glycine-rich sequence, HRD and DLG motifs are in purple, and the conserved residues K⁷⁴ (β3 strand) and E⁹³ (αC helix) are in red. The putative nuclear export signal LGDLGL based on la Cour et al., 2004 [63], is underlined and the putative WW domain binding motifs PY and pSP based on Ingham et al., 2005 [64], as well as the PPLP motif experimentally described for hNek6 by Lee et al., 2007 [65], are indicated by dotted lines. Putative phosphorylation sites were predicted by NetPhosK 1.0 software and are indicated in blue; S²⁰⁶ in hNek6 is also indicated because of previously described phosphorylation of this residue by hNek9 [13]. These motifs are also present in Nek7 amino acid sequence. The author-approved secondary structure of hNek7 in PDB (2WQM) is also depicted. (C) Primary sequence alignment between human Nek6 (NP_055212.2) and Nek7 (NP_598001.1) using Clustal W2. The N-terminal regulatory domain is highlighted in yellow.